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[omega]-1 and [omega]-2 hydroxylation of prostaglandins by rabbit hepatic microsomal cytochrome P-450 isozyme 6

dc.contributor.authorHolm, Karsten A.en_US
dc.contributor.authorKoop, Dennis R.en_US
dc.contributor.authorCoon, Minor J.en_US
dc.contributor.authorTheoharides, Anthony D.en_US
dc.contributor.authorKupfer, Daviden_US
dc.date.accessioned2006-04-07T18:54:12Z
dc.date.available2006-04-07T18:54:12Z
dc.date.issued1985-11-15en_US
dc.identifier.citationHolm, Karsten A., Koop, Dennis R., Coon, Minor J., Theoharides, Anthony D., Kupfer, David (1985/11/15)."[omega]-1 and [omega]-2 hydroxylation of prostaglandins by rabbit hepatic microsomal cytochrome P-450 isozyme 6." Archives of Biochemistry and Biophysics 243(1): 135-143. <http://hdl.handle.net/2027.42/25496>en_US
dc.identifier.urihttp://www.sciencedirect.com/science/article/B6WB5-4DXBDXY-H/2/b07aa5eaf0a69ca323783911f69da8ecen_US
dc.identifier.urihttps://hdl.handle.net/2027.42/25496
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=3864395&dopt=citationen_US
dc.description.abstractIncubation of prostaglandin E1 (PGE1) with liver microsomes from control rabbits and from rabbits treated with ethanol or imidazole yielded 18-, 19-, and 20-hydroxy metabolites, representing hydroxylation at [omega]-2, [omega]-1, and [omega] carbons, respectively. The current investigation demonstrates that rabbit liver P-450 isozyme 6 effectively catalyzes the [omega]-1 andg w-2 hydroxylation of PGE1 and PGE2. Additionally, a small amount of product with Chromatographic characteristics of the corresponding 20-hydroxy metabolite has been detected. The incorporation of cytochrome b5 into the reconstituted system did not enhance the rate of PGE1 hydroxylation and had no effect on the ratio of products formed. The Km value for the [omega]-1 and [omega]-2 hydroxylation of PGE1 with P-450 isozyme 6 from imidazole-treated rabbits was approximately 140 [mu]; the Vmax's (nmol product min-1 nmol P-450-1) were 2.1 and 1.1 for the [omega]-1 and [omega]-2 hydroxylations, respectively. These rates represent the highest activities by hepatic P-450 isozymes for hydroxylation of PGs, and suggest that isozyme 6 is responsible for the [omega]-2 hydroxylation of PGEs observed in rabbit liver microsomes.en_US
dc.format.extent1385214 bytes
dc.format.extent3118 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.language.isoen_US
dc.publisherElsevieren_US
dc.title[omega]-1 and [omega]-2 hydroxylation of prostaglandins by rabbit hepatic microsomal cytochrome P-450 isozyme 6en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelPublic Healthen_US
dc.subject.hlbsecondlevelChemistryen_US
dc.subject.hlbsecondlevelChemical Engineeringen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelEngineeringen_US
dc.subject.hlbtoplevelScienceen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationumDepartment of Biological Chemistry, University of Michigan Medical School, Ann Arbor, Michigan 48109, USAen_US
dc.contributor.affiliationotherWorcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545, USAen_US
dc.contributor.affiliationotherDivision of Experimental Therapeutics, Walter Reed Army Institute of Research, Washington, D. C., USAen_US
dc.contributor.affiliationotherWorcester Foundation for Experimental Biology, Shrewsbury, Massachusetts 01545, USAen_US
dc.identifier.pmid3864395en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/25496/1/0000037.pdfen_US
dc.identifier.doihttp://dx.doi.org/10.1016/0003-9861(85)90781-7en_US
dc.identifier.sourceArchives of Biochemistry and Biophysicsen_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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